Aminophospholipid translocase and proteins involved in transmembrane phospholipid traffic.
The transmembrane distribution of phospholipids in the membranes of eukaryotic cells depends on specific proteins (called flippases). The aminophospholipid translocase is responsible for the sequestration of phosphatidylserine and phosphatidylethanolamine in the cytosolic leaflet of plasma membranes. Several laboratories are presently working on the identification, purification and cloning of this Mg-ATPase, first recognized in the human red cell membrane. In accordance with the 1992 hypothesis of Higgins and Gottesman, proteins of the MDR1 family appear to be able to translocate certain phospholipids from the inner to the outer monolayer of the plasma membrane. It has been reported in particular that expression of the human MDR3 and mouse mdr2 genes promote translocation of long chain phosphatidylcholine, while expression of the MDR1 gene stimulates the outward motion of phospholipids possessing at least one short chain. ATP-independent flippases activities were recognized not only in microsomes but also in Golgi membranes.
Dolis
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Institut de Biologie Physico-Chimique, Paris, France.
Moreau
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Zachowski
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Devaux
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PF
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D049294:Phospholipid Transfer Proteins; D010743:Phospholipids / Q000378:metabolism*
D002352:Carrier Proteins; D008565:Membrane Proteins; D049294:Phospholipid Transfer Proteins; D010743:Phospholipids